Analyses of interactions between heparin and the apical surface proteins of plasmodium falciparum

Kyousuke Kobayashi, Ryo Takano, Hitoshi Takemae, Tatsuki Sugi, Akiko Ishiwa, Haiyan Gong, Frances C. Recuenco, Tatsuya Iwanaga, Taisuke Horimoto, Hiroomi Akashi, Kentaro Kato

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)

Abstract

Heparin, a sulfated glycoconjugate, reportedly inhibits the blood-stage growth of the malaria parasite Plasmodium falciparum. Elucidation of the inhibitory mechanism is valuable for developing novel invasion-blocking treatments based on heparin. Merozoite surface protein 1 has been reported as a candidate target of heparin; however, to better understand the molecular mechanisms involved, we characterized the molecules that bind to heparin during merozoite invasion. Here, we show that heparin binds only at the apical tip of the merozoite surface and that multiple heparin-binding proteins localize preferentially in the apical organelles. To identify heparin-binding proteins, parasite proteins were fractionated by means of heparin affinity chromatography and subjected to immunoblot analysis with ligand-specific antibodies. All tested members of the Duffy and reticulocyte binding-like families bound to heparin with diverse affinities. These findings suggest that heparin masks the apical surface of merozoites and blocks interaction with the erythrocyte membrane after initial attachment.

Original languageEnglish
Article number3178
JournalScientific reports
Volume3
DOIs
Publication statusPublished - 2013

ASJC Scopus subject areas

  • General

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